NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
TISSUE=Leaf;
PubMed=7983054 [NCBI, ExPASy, EBI, Israel, Japan]
Murthy S.S., Zilinskas B.A.;
"Molecular cloning and characterization of a cDNA encoding pea monodehydroascorbate reductase.";
J. Biol. Chem. 269:31129-31133(1994).

Comments

FUNCTION: Catalyzes the conversion of monodehydroascorbate to ascorbate, oxidizing NADH in the process.
CATALYTIC ACTIVITY: NADH + 2 monodehydroascorbate = NAD⁺ + 2 ascorbate.
COFACTOR: FAD (By similarity).

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=5.3 µM for NADH;
	K_M=21.5 µM for NADPH;
	K_M=5.7 µM for monodehydroascorbate;
	V_max=312 µmol/min/mg enzyme for NADH oxidation reaction;
	V_max=40.9 µmol/min/mg enzyme for NADPH oxidation reaction;
pH dependence:	Optimum pH is 7.5-9.5;

SUBCELLULAR LOCATION: Cytoplasm (Probable).
TISSUE SPECIFICITY: Expressed at relatively low levels in all tissues examined.
SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U06461; AAA60979.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A55333; A55333.

3D structure databases

HSSP

Q94655; 1ONF. [HSSP ENTRY / PDB]

ModBase

Q40977.

Ontologies

GO:0016656;	Molecular function: monodehydroascorbate reductase (NADH) activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00411; PNDRDTASEI.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 433`	`433`	`Monodehydroascorbate reductase.`	`PRO_0000209143`
`NP_BIND`	`6 23`	`18`	`FAD (By similarity).`
`NP_BIND`	`164 181`	`18`	`NAD (By similarity).`
`NP_BIND`	`190 194`	`5`	`FAD (By similarity).`

Sequence information

Length: 433 AA [This is the length of the unprocessed precursor]

Molecular weight: 47309 Da [This is the MW of the unprocessed precursor]

CRC64: 5435C1F9E2BFCC97 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVHSFKYIII GGGVSAGYAA REFVKQGVHP GELAIISKEA VAPYERPALS KAYLFPESPA 

        70         80         90        100        110        120 
RLPGFHTCVG SGGERLLPEW YSEKGIQLYL STEIVSADLA AKFLKSANGE HFDYQTLVIA 

       130        140        150        160        170        180 
TGSAVIRLTD FGVIGANAKN IFYLREVDDA DKLYEAIKRK KNAKRVVVGG GYIGLELSAV 

       190        200        210        220        230        240 
LKLNDLDVTM VYPEPWCMPR LFTSEIAAFY EGYYANKGIN IIKGTVAVGF TANSDGEVKE 

       250        260        270        280        290        300 
VKLKDGRVLE ADIVIVGVGG RPQISLFKGQ VEEQHGGIKT DSFFKTSVPD VYAVGDVATF 

       310        320        330        340        350        360 
PLKLYNDVRR VEHVDHARKS AEQAAKAIFA ADVGKSVEEY DYLPYFYSRS FDLSWQFYGD 

       370        380        390        400        410        420 
NVGETVLFGD NDPASSKPKF GTYWIKEGKV VGAFLEGGTP DENKAIAKVA RAKPAVEDVN 

       430 
QLAEEGLSFA SKI

Q40977 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools